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Virology. 1991 Feb;180(2):617-24.

Structural characteristics of the M2 protein of influenza A viruses: evidence that it forms a tetrameric channel.

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National Institute for Medical Research, Mill Hill, London, United Kingdom.


The evidence presented shows that the M2 protein of influenza A viruses exists in infected cells as a homotetramer composed of two disulfide-linked dimers held together by noncovalent interactions. The amphiphilic nature of the transmembrane alpha-helical domain is consistent with the protein forming a transmembrane channel with which amantadine, the specific anti-influenza A drug, interacts. Together these features provide a structural basis for the hypothesis that M2 has a proton translocation function capable of regulating the pH of vesicles of the trans-Golgi network, a role important in promoting the correct maturation of the hemagglutinin glycoprotein.

[Indexed for MEDLINE]

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